title: Steady-state fluorescence polarization/anisotropy for the study of protein interactions.
abstract: Fluorescence methods are often employed for the characterization of molecular interactions. In particular, polarization/anisotropy studies are widely utilized in the life sciences as they allow quantification of protein interactions in the micro- and nanomolar concentration range. Herein we shall briefly describe the theoretical aspects of polarization/anisotropy and outline an experiment for determination of the dissociation constant for a protein-ligand complex.
authors.affiliation: Department Cell and Molecular Biology, John A. Burns School of Medicine, University of Hawaii, Honolulu, HI, USA.
authors.forename: Nicholas G
authors.initials: NG
authors.lastname: James
authors.forename: David M
authors.initials: DM
authors.lastname: Jameson
mesh_terms: D016880:Anisotropy; D005454:Fluorescence Polarization / Q000379:methods*; D005456:Fluorescent Dyes / Q000737:chemistry*; D008024:Ligands; D060066:Protein Interaction Maps; D011506:Proteins / Q000737:chemistry*; D013050:Spectrometry, Fluorescence
chemical_list: D005456:Fluorescent Dyes; D008024:Ligands; D011506:Proteins